Difference between revisions of "Part:BBa K3782000"
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− | FfIBP is a protein coding region that codes for an ice binding protein (IBP). IBPs, or more specifically antifreeze proteins (AFP), can bind to ice crystals and thereby prevent further ice growth. They are produced by organisms to survive in extremely cold environments. Activities of AFPs can be characterized by their thermal hysteresis (TH) or by their ice recrystallization inhibition (IRI). TH activity corresponds to the lowering of the freezing point without changing the melting point of a solution. IRI activity inhibits the growth of large ice crystals at the expense of smaller ones. The combination of these activities, which vary depending on the protein structure, prevents the freezing of body fluids and cell damage in organisms that live in environments with extremely cold temperatures. | + | <partinfo>BBa_K3782000 short</partinfo> |
+ | =FfIBP= | ||
+ | '''FfIBP''' is a protein coding region that codes for an ice binding protein (IBP). IBPs, or more specifically antifreeze proteins (AFP), can bind to ice crystals and thereby prevent further ice growth. They are produced by organisms to survive in extremely cold environments. Activities of AFPs can be characterized by their thermal hysteresis (TH) or by their ice recrystallization inhibition (IRI). TH activity corresponds to the lowering of the freezing point without changing the melting point of a solution. IRI activity inhibits the growth of large ice crystals at the expense of smaller ones. The combination of these activities, which vary depending on the protein structure, prevents the freezing of body fluids and cell damage in organisms that live in environments with extremely cold temperatures. | ||
− | FfIBP is naturally produced by the Gram-negative Antarctic bacterium Flavobacterium frigoris PS1. Its TH activity is around 2.5 K at 50 µM. | + | __TOC__ |
+ | |||
+ | =Profile= | ||
+ | <html> | ||
+ | <table style=“width:80%“> | ||
+ | <tr> | ||
+ | <td><b>Name</b></td> | ||
+ | <td>FfIBP </td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><b>Base pairs</b></td> | ||
+ | <td>744</td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><b>Number of amino acids</b></td> | ||
+ | <td>247</td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><b>Molecular weight</b></td> | ||
+ | <td>25.35 kDa</td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><b>Origin</b></td> | ||
+ | <td><i>Flavobacterium frigoris</i> strain PS1, synthetic</td> | ||
+ | </tr> | ||
+ | </table> | ||
+ | </html> | ||
+ | =Usage and Biology= | ||
+ | =Characterization= | ||
+ | =Sequence and Features= | ||
+ | <partinfo>BBa_K3782000 SequenceAndFeatures</partinfo> | ||
+ | =References= | ||
+ | |||
+ | FfIBP is naturally produced by the Gram-negative Antarctic bacterium <i>Flavobacterium frigoris</i> PS1. Its TH activity is around 2.5 K at 50 µM. |
Revision as of 13:53, 9 October 2021
Flavobacterium frigoris strain PS1 ice-binding protein gene
FfIBP
FfIBP is a protein coding region that codes for an ice binding protein (IBP). IBPs, or more specifically antifreeze proteins (AFP), can bind to ice crystals and thereby prevent further ice growth. They are produced by organisms to survive in extremely cold environments. Activities of AFPs can be characterized by their thermal hysteresis (TH) or by their ice recrystallization inhibition (IRI). TH activity corresponds to the lowering of the freezing point without changing the melting point of a solution. IRI activity inhibits the growth of large ice crystals at the expense of smaller ones. The combination of these activities, which vary depending on the protein structure, prevents the freezing of body fluids and cell damage in organisms that live in environments with extremely cold temperatures.
Contents
Profile
Name | FfIBP |
Base pairs | 744 |
Number of amino acids | 247 |
Molecular weight | 25.35 kDa |
Origin | Flavobacterium frigoris strain PS1, synthetic |
Usage and Biology
Characterization
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 269
Illegal PstI site found at 350
Illegal PstI site found at 530 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 269
Illegal PstI site found at 350
Illegal PstI site found at 530 - 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 269
Illegal PstI site found at 350
Illegal PstI site found at 530 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 269
Illegal PstI site found at 350
Illegal PstI site found at 530 - 1000COMPATIBLE WITH RFC[1000]
References
FfIBP is naturally produced by the Gram-negative Antarctic bacterium Flavobacterium frigoris PS1. Its TH activity is around 2.5 K at 50 µM.